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| | ==NMR STRUCTURE OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES== | | ==NMR STRUCTURE OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES== |
| - | <StructureSection load='1q9g' size='340' side='right' caption='[[1q9g]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1q9g' size='340' side='right'caption='[[1q9g]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1q9g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q9G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1q9g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q9G FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1orm|1orm]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OMPX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q9g OCA], [https://pdbe.org/1q9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q9g RCSB], [https://www.ebi.ac.uk/pdbsum/1q9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q9g ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q9g OCA], [http://pdbe.org/1q9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q9g RCSB], [http://www.ebi.ac.uk/pdbsum/1q9g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q9g ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/OMPX_ECOLI OMPX_ECOLI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Fernandez, C]] | + | [[Category: Large Structures]] |
| - | [[Category: Guntert, P]] | + | [[Category: Fernandez C]] |
| - | [[Category: Hilty, C]] | + | [[Category: Guntert P]] |
| - | [[Category: Wider, G]] | + | [[Category: Hilty C]] |
| - | [[Category: Wuthrich, K]] | + | [[Category: Wider G]] |
| - | [[Category: Detergent]]
| + | [[Category: Wuthrich K]] |
| - | [[Category: Dhpc]]
| + | |
| - | [[Category: Lipid]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Micelle]]
| + | |
| - | [[Category: Ompx]]
| + | |
| - | [[Category: Trosy]]
| + | |
| Structural highlights
Function
OMPX_ECOLI
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of the integral membrane protein OmpX from Escherichia coli reconstituted in 60 kDa DHPC micelles (OmpX/DHPC) was calculated from 526 NOE upper limit distance constraints. The structure determination was based on complete sequence-specific assignments for the amide protons and the Val, Leu, and Ile(delta1) methyl groups in OmpX, which were selectively protonated on a perdeuterated background. The solution structure of OmpX in the DHPC micelles consists of a well-defined, eight-stranded antiparallel beta-barrel, with successive pairs of beta-strands connected by mobile loops. Several long-range NOEs observed outside of the transmembrane barrel characterize an extension of a four-stranded beta-sheet beyond the height of the barrel. This protruding beta-sheet is believed to be involved in intermolecular interactions responsible for the biological functions of OmpX. The present approach for de novo structure determination should be quite widely applicable to membrane proteins reconstituted in mixed micelles with overall molecular masses up to about 100 kDa, and may also provide a platform for additional functional studies.
NMR structure of the integral membrane protein OmpX.,Fernandez C, Hilty C, Wider G, Guntert P, Wuthrich K J Mol Biol. 2004 Mar 5;336(5):1211-21. PMID:15037080[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fernandez C, Hilty C, Wider G, Guntert P, Wuthrich K. NMR structure of the integral membrane protein OmpX. J Mol Biol. 2004 Mar 5;336(5):1211-21. PMID:15037080 doi:10.1016/j.jmb.2003.09.014
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